Goldsmith M A, Dazin P F, Weiss A
Department of Medicine, School of Medicine, University of California, San Francisco 94143.
Proc Natl Acad Sci U S A. 1988 Nov;85(22):8613-7. doi: 10.1073/pnas.85.22.8613.
In the T-cell somatic mutant J.CaM1, the T-cell antigen receptor complex is poorly coupled to the inositolphospholipid second messenger system; some antibodies against the invariant CD3 subunit of the receptor retain their agonist function in J.CaM1. Here we show by a combination of complementation assays that the mutation in J.CaM1 affects a molecule other than the antigen-binding Ti subunit, suggesting that Ti is coupled indirectly to the signal transduction apparatus through a pathway involving the CD3 complex. We also describe another mutant, J.CaM2, in which the receptor complex is completely uncoupled from inositolphospholipid hydrolysis. J.CaM2 defines an additional complementation group, suggesting that signal transduction by the antigen receptor depends on at least two molecules distinct from Ti.
在T细胞体细胞突变体J.CaM1中，T细胞抗原受体复合物与肌醇磷脂第二信使系统的偶联较差；一些针对受体恒定CD3亚基的抗体在J.CaM1中保留了它们的激动剂功能。在此我们通过互补分析表明，J.CaM1中的突变影响的分子不是抗原结合性Ti亚基，这表明Ti是通过涉及CD3复合物的途径间接与信号转导装置偶联的。我们还描述了另一个突变体J.CaM2，其中受体复合物与肌醇磷脂水解完全解偶联。J.CaM2定义了一个额外的互补群，这表明抗原受体的信号转导至少依赖于两个不同于Ti的分子。
